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RAB1320

Sigma-Aldrich

人组织蛋白酶Z ELISA

for serum, plasma and cell culture supernatants

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About This Item

分類程式碼代碼:
12352200

物種活性

human

技術

ELISA: suitable

輸入

sample type serum
sample type plasma
sample type cell culture supernatant(s)

assay range

inter-assay cv: <12%
intra-assay cv: <10%

運輸包裝

wet ice

儲存溫度

−20°C

基因資訊

human ... CTSZ(1522)

一般說明

Cathepsins are normally localized in lysosomes of almost all mammalian cells, but under certain conditions they can be secreted from the cells that take part in local proteolysis. Cathepsin Z is a cysteine protease, predominantly expressed in immune cells including monocytes, macrophages or dendritic cells.
This ELISA antibody pair detects Human Cathepsin Z (CTSZ/Cathepsin X/Cathepsin P)

應用

For research use only. Not for use in diagnostic procedures.
Please refer to the attached Protocolfor details.

生化/生理作用

Cathepsins are lysosomal proteases that play an important role in the intracellular degradation of exogenous and endogenous proteins, activation of enzyme precursors, and tumor invasion and metastasis. Cathepsin Z is known to be associated with the pathogenesis of cancer and promotes the development and proliferation of tumor cells. Cathepsin Z mediates the process of proliferation, migration, maturation, adhesion, signal transduction and phagocytosis of immune cells.

其他說明

A sample Certificate of Analysis is available for this product. Please type the word sample in the text box provided for lot number.

象形圖

Corrosion

訊號詞

Warning

危險聲明

防範說明

危險分類

Met. Corr. 1

儲存類別代碼

8A - Combustible corrosive hazardous materials

閃點(°F)

Not applicable

閃點(°C)

Not applicable


分析證明 (COA)

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Cysteine cathepsins B and X promote epithelial-mesenchymal transition of tumor cells.
Mitrovic A, et al.
European Journal of Cell Biology, 96(6), 622-631 (2017)
Localization and activity of various lysosomal proteases in Leishmania amazonensis-infected macrophages.
Prina E R I C, et al.
Infection and Immunity, 58(6), 1730-1737 (1990)
Dysregulation of apoptotic signaling pathways by interaction of RPLP0 and cathepsin X/Z in gastric cancer.
Teller A, et al.
Pathology Research and Practice, 211(1), 62-70 (2015)
Cysteine cathepsins and the cutting edge of cancer invasion.
Gocheva V and Joyce J A
Cell Cycle, 6(1), 60-64 (2007)
L Polgár et al.
The Journal of biological chemistry, 262(30), 14448-14453 (1987-10-25)
Negatively charged reactants are sensitive reactivity probes of the active site of cysteine proteases (Halász, P., and Polgár, L. (1977) Eur. J. Biochem. 79, 491-494). Thus, the thiolate-imidazolium ion pair of papain reacts at an enhanced rate with iodoacetate due

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